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Protein

Guanine nucleotide exchange factor VAV2

Gene

Vav2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Guanine nucleotide exchange factor for the Rho family of Ras-related GTPases. Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri513 – 56250Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: MGI
  • guanyl-nucleotide exchange factor activity Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • Rho guanyl-nucleotide exchange factor activity Source: InterPro

GO - Biological processi

  • angiogenesis Source: UniProtKB-KW
  • cell migration Source: MGI
  • cell projection assembly Source: MGI
  • lamellipodium assembly Source: MGI
  • platelet activation Source: Reactome
  • positive regulation of phosphatidylinositol 3-kinase activity Source: MGI
  • regulation of blood coagulation Source: MGI
  • regulation of cell size Source: Ensembl
  • regulation of gene expression Source: MGI
  • regulation of GTPase activity Source: MGI
  • regulation of Rho protein signal transduction Source: InterPro
  • small GTPase mediated signal transduction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Angiogenesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-114604. GPVI-mediated activation cascade.
R-MMU-193648. NRAGE signals death through JNK.
R-MMU-194840. Rho GTPase cycle.
R-MMU-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-MMU-2424491. DAP12 signaling.
R-MMU-2871796. FCERI mediated MAPK activation.
R-MMU-2871809. FCERI mediated Ca+2 mobilization.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.
R-MMU-416482. G alpha (12/13) signalling events.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-445144. Signal transduction by L1.
R-MMU-5218920. VEGFR2 mediated vascular permeability.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide exchange factor VAV2
Short name:
VAV-2
Gene namesi
Name:Vav2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:102718. Vav2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • plasma membrane Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 868868Guanine nucleotide exchange factor VAV2PRO_0000080985Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei142 – 1421Phosphotyrosine; by EGFRBy similarity
Modified residuei159 – 1591Phosphotyrosine; by EGFRBy similarity
Modified residuei172 – 1721Phosphotyrosine; by EGFRBy similarity
Modified residuei566 – 5661PhosphoserineBy similarity
Modified residuei616 – 6161PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on tyrosine residues in response to FGR activation.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ60992.
PaxDbiQ60992.
PeptideAtlasiQ60992.
PRIDEiQ60992.

PTM databases

iPTMnetiQ60992.
PhosphoSiteiQ60992.

Expressioni

Gene expression databases

BgeeiENSMUSG00000009621.
CleanExiMM_VAV2.
ExpressionAtlasiQ60992. baseline and differential.
GenevisibleiQ60992. MM.

Interactioni

Subunit structurei

Interacts (via SH2 domains) with the phosphorylated form of EPHA2. Interacts with NEK3 and PRLR and this interaction is prolactin-dependent (By similarity). Interacts with SSX2IP.By similarity2 Publications

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: MGI

Protein-protein interaction databases

IntActiQ60992. 4 interactions.
MINTiMINT-85279.
STRINGi10090.ENSMUSP00000062782.

Structurei

3D structure databases

ProteinModelPortaliQ60992.
SMRiQ60992. Positions 1-562, 579-868.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 119119CHPROSITE-ProRule annotationAdd
BLAST
Domaini193 – 371179DHPROSITE-ProRule annotationAdd
BLAST
Domaini400 – 502103PHPROSITE-ProRule annotationAdd
BLAST
Domaini576 – 64267SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini663 – 75795SH2PROSITE-ProRule annotationAdd
BLAST
Domaini806 – 86762SH3 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 2 SH3 domains.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri513 – 56250Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, SH2 domain, SH3 domain, Zinc-finger

Phylogenomic databases

eggNOGiKOG2996. Eukaryota.
ENOG410XPH6. LUCA.
GeneTreeiENSGT00800000124085.
HOGENOMiHOG000234364.
HOVERGENiHBG018066.
InParanoidiQ60992.
KOiK05730.
OMAiPGPKMVA.
OrthoDBiEOG091G01O3.
PhylomeDBiQ60992.
TreeFamiTF316171.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR022613. CAMSAP_CH.
IPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR028530. Vav.
[Graphical view]
PANTHERiPTHR22826:SF95. PTHR22826:SF95. 2 hits.
PfamiPF00130. C1_1. 1 hit.
PF11971. CAMSAP_CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
PF07653. SH3_2. 2 hits.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 2 hits.
SSF50729. SSF50729. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50021. CH. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60992-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQWRQCGRW LIDCKVLPPN HRVVWPSAVV FDLAQALRDG VLLCQLLHNL
60 70 80 90 100
SPGSIDLKDI NFRPQMSQFL CLKNIRTFLK VCHDKFGLRN SELFDPFDLF
110 120 130 140 150
DVRDFGKVIS AVSRLSLHSI AQSKGIRPFP SEETAENDDD VYRSLEELAD
160 170 180 190 200
EHDLGEDIYD CVPCEDEGDD IYEDIIKVEV QQPMKMGMTE DDKRSCCLLE
210 220 230 240 250
IQETEAKYYR TLEDIEKNYM GPLRLVLSPA DMAAVFINLE DLIKVHHSFL
260 270 280 290 300
RAIDVSMMAG GSTLAKVFLE FKERLLIYGE YCSHMEHAQS TLNQLLASRE
310 320 330 340 350
DFRQKVEECT LRVQDGKFKL QDLLVVPMQR VLKYHLLLKE LLSHSADRPE
360 370 380 390 400
RQQLKEALEA MQDLAMYINE VKRDKETLKK ISEFQCSIEN LQVKLEEFGR
410 420 430 440 450
PKIDGELKVR SIVNHTKQDR YLFLFDKVVI VCKRKGYSYE LKEVIELLFH
460 470 480 490 500
KMTDDPMHNK DIKKWSYGFY LIHLQGKQGF QFFCKTEDMK RKWMEQFEMA
510 520 530 540 550
MSNIKPDKAN ANHHSFQMYT FDKTTNCKAC KMFLRGTFYQ GYLCTRCGVG
560 570 580 590 600
AHKECLEVIP PCKMSSPADV DAPGAGPGPK MVAVQNYHGN PAPPGKPVLT
610 620 630 640 650
FQTGDVIELL RGDPDSPWWE GRLVQTRKSG YFPSSSVKPC PVDGRPPTGR
660 670 680 690 700
PPSREIDYTA YPWFAGNMER QQTDNLLKSH ASGTYLIRER PAEAERFAIS
710 720 730 740 750
IKFNDEVKHI KVVEKDSWIH ITEAKKFESL LELVEYYQCH SLKESFKQLD
760 770 780 790 800
TTLKFPYKSR ERTTSRASSR SPASCASYNF SFLSPQGLSF APQAPSAPFW
810 820 830 840 850
SVFTPRVIGT AVARYNFAAR DMRELSLREG DVVKIYSRIG GDQGWWKGET
860
NGRIGWFPST YVEEEGVQ
Length:868
Mass (Da):99,915
Last modified:November 1, 1997 - v1
Checksum:iD18581E7EEB2DBC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37017 mRNA. Translation: AAC52761.1.
AL731552, AL772282 Genomic DNA. Translation: CAM13732.1.
AL772282, AL731552 Genomic DNA. Translation: CAM21000.1.
CCDSiCCDS15827.1.
RefSeqiNP_033526.1. NM_009500.2.
UniGeneiMm.179011.

Genome annotation databases

EnsembliENSMUST00000056176; ENSMUSP00000062782; ENSMUSG00000009621.
GeneIDi22325.
KEGGimmu:22325.
UCSCiuc008ixh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37017 mRNA. Translation: AAC52761.1.
AL731552, AL772282 Genomic DNA. Translation: CAM13732.1.
AL772282, AL731552 Genomic DNA. Translation: CAM21000.1.
CCDSiCCDS15827.1.
RefSeqiNP_033526.1. NM_009500.2.
UniGeneiMm.179011.

3D structure databases

ProteinModelPortaliQ60992.
SMRiQ60992. Positions 1-562, 579-868.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ60992. 4 interactions.
MINTiMINT-85279.
STRINGi10090.ENSMUSP00000062782.

PTM databases

iPTMnetiQ60992.
PhosphoSiteiQ60992.

Proteomic databases

MaxQBiQ60992.
PaxDbiQ60992.
PeptideAtlasiQ60992.
PRIDEiQ60992.

Protocols and materials databases

DNASUi22325.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056176; ENSMUSP00000062782; ENSMUSG00000009621.
GeneIDi22325.
KEGGimmu:22325.
UCSCiuc008ixh.1. mouse.

Organism-specific databases

CTDi7410.
MGIiMGI:102718. Vav2.

Phylogenomic databases

eggNOGiKOG2996. Eukaryota.
ENOG410XPH6. LUCA.
GeneTreeiENSGT00800000124085.
HOGENOMiHOG000234364.
HOVERGENiHBG018066.
InParanoidiQ60992.
KOiK05730.
OMAiPGPKMVA.
OrthoDBiEOG091G01O3.
PhylomeDBiQ60992.
TreeFamiTF316171.

Enzyme and pathway databases

ReactomeiR-MMU-114604. GPVI-mediated activation cascade.
R-MMU-193648. NRAGE signals death through JNK.
R-MMU-194840. Rho GTPase cycle.
R-MMU-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-MMU-2424491. DAP12 signaling.
R-MMU-2871796. FCERI mediated MAPK activation.
R-MMU-2871809. FCERI mediated Ca+2 mobilization.
R-MMU-3928665. EPH-ephrin mediated repulsion of cells.
R-MMU-416482. G alpha (12/13) signalling events.
R-MMU-4420097. VEGFA-VEGFR2 Pathway.
R-MMU-445144. Signal transduction by L1.
R-MMU-5218920. VEGFR2 mediated vascular permeability.

Miscellaneous databases

ChiTaRSiVav2. mouse.
PROiQ60992.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000009621.
CleanExiMM_VAV2.
ExpressionAtlasiQ60992. baseline and differential.
GenevisibleiQ60992. MM.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR022613. CAMSAP_CH.
IPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR028530. Vav.
[Graphical view]
PANTHERiPTHR22826:SF95. PTHR22826:SF95. 2 hits.
PfamiPF00130. C1_1. 1 hit.
PF11971. CAMSAP_CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
PF07653. SH3_2. 2 hits.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 2 hits.
SSF50729. SSF50729. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50021. CH. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVAV2_MOUSE
AccessioniPrimary (citable) accession number: Q60992
Secondary accession number(s): A2AH49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.